ITA5_HUMAN - dbPTM
ITA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA5_HUMAN
UniProt AC P08648
Protein Name Integrin alpha-5
Gene Name ITGA5
Organism Homo sapiens (Human).
Sequence Length 1049
Subcellular Localization Membrane
Single-pass type I membrane protein. Cell junction, focal adhesion . Cell surface .
Protein Description Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. [PubMed: 18635536]
Protein Sequence MGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLDDLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQILLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEAELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGASLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQVTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQQKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVWAKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKAEGSYGVPLWIIILAILFGLLLLGLLIYILYKLGFFKRSLPYGTAMEKAQLKPPATSDA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
84N-linked_GlycosylationLVGAPKANTSQPGVL
EECCCCCCCCCCCEE		46.5222451694
123PhosphorylationKGSRLLESSLSSSEG
CCCHHHHHHCCCCCC		36.2322167270
124PhosphorylationGSRLLESSLSSSEGE
CCHHHHHHCCCCCCC		23.9322167270
126PhosphorylationRLLESSLSSSEGEEP
HHHHHHCCCCCCCCC		33.4922167270
127PhosphorylationLLESSLSSSEGEEPV
HHHHHCCCCCCCCCC		37.3922167270
128PhosphorylationLESSLSSSEGEEPVE
HHHHCCCCCCCCCCE		46.3619664994
133N-linked_GlycosylationSSSEGEEPVEYKSLQ
CCCCCCCCCEECEEE		21.6722451694
137UbiquitinationGEEPVEYKSLQWFGA
CCCCCEECEEEEECC		31.0521906983
164PhosphorylationAPLYSWRTEKEPLSD
CCCCEECCCCCCCCC		45.1927251275
166UbiquitinationLYSWRTEKEPLSDPV
CCEECCCCCCCCCCC		65.11-
170PhosphorylationRTEKEPLSDPVGTCY
CCCCCCCCCCCCEEE		51.0527251275
172PhosphorylationEKEPLSDPVGTCYLS
CCCCCCCCCCEEEEE		24.06-
173PhosphorylationKEPLSDPVGTCYLST
CCCCCCCCCEEEEEC		13.72-
175PhosphorylationPLSDPVGTCYLSTDN
CCCCCCCEEEEECCC		9.7527251275
176PhosphorylationLSDPVGTCYLSTDNF
CCCCCCEEEEECCCC		2.3718578522
177PhosphorylationSDPVGTCYLSTDNFT
CCCCCEEEEECCCCC		11.9719664994
179PhosphorylationPVGTCYLSTDNFTRI
CCCEEEEECCCCCHH		13.7727251275
180PhosphorylationVGTCYLSTDNFTRIL
CCEEEEECCCCCHHH		32.1627251275
182N-linked_GlycosylationTCYLSTDNFTRILEY
EEEEECCCCCHHHHC		40.0317660510
186UbiquitinationSTDNFTRILEYAPCR
ECCCCCHHHHCCCCC		2.89-
210PhosphorylationGYCQGGFSAEFTKTG
CCCCCCCEEEEEECC		30.1129507054
215UbiquitinationGFSAEFTKTGRVVLG
CCEEEEEECCCEEEC		55.06-
231N-linked_GlycosylationPGSYFWQGQILSATQ
CCCCCCCCCCCHHCH		13.6922451694
259PhosphorylationNLVQGQLQTRQASSI
HHHHHHCCCCCCCCC		27.10-
274PhosphorylationYDDSYLGYSVAVGEF
CCCCCCCEEEEEEEC		9.4422210691
275PhosphorylationDDSYLGYSVAVGEFS
CCCCCCEEEEEEECC		11.2122210691
297N-linked_GlycosylationVAGVPKGNLTYGYVT
CCCCCCCCEEEEEEE		35.0222451694
304PhosphorylationNLTYGYVTILNGSDI
CEEEEEEEEECCCHH		15.9722210691
307N-linked_GlycosylationYGYVTILNGSDIRSL
EEEEEEECCCHHHHH		44.0322451694
309PhosphorylationYVTILNGSDIRSLYN
EEEEECCCHHHHHCC		28.8822210691
316N-linked_GlycosylationSDIRSLYNFSGEQMA
CHHHHHCCCCHHHHH		29.8722451694
346N-linked_GlycosylationGLDDLLVGAPLLMDR
CHHHHCCCCCEEEEC		22.8019349973
346N-linked_GlycosylationGLDDLLVGAPLLMDR
CHHHHCCCCCEEEEC		22.8019349973
354PhosphorylationAPLLMDRTPDGRPQE
CCEEEECCCCCCCCC		22.8229052541
356N-linked_GlycosylationLLMDRTPDGRPQEVG
EEEECCCCCCCCCCC		66.1819349973
356N-linked_GlycosylationLLMDRTPDGRPQEVG
EEEECCCCCCCCCCC		66.1819349973
365N-linked_GlycosylationRPQEVGRVYVYLQHP
CCCCCCEEEEEEECC		2.8922451694
394PhosphorylationDEFGRFGSSLTPLGD
CCCCCCCCCCCCCCC		21.33-
395PhosphorylationEFGRFGSSLTPLGDL
CCCCCCCCCCCCCCC		36.32-
471PhosphorylationRDLDGNGYPDLIVGS
CCCCCCCCCCEEEEE		9.5126699800
478PhosphorylationYPDLIVGSFGVDKAV
CCCEEEEEECCCEEE		14.1326699800
487PhosphorylationGVDKAVVYRGRPIVS
CCCEEEEECCCCEEE		10.76-
524N-linked_GlycosylationGNPVACINLSFCLNA
CCCEEEEEEEEEECC		29.53UniProtKB CARBOHYD
530N-linked_GlycosylationINLSFCLNASGKHVA
EEEEEEECCCCCCCH		32.99UniProtKB CARBOHYD
593N-linked_GlycosylationEMKIYLRNESEFRDK
HCEEEECCHHHHHHH		55.33UniProtKB CARBOHYD
609N-linked_GlycosylationSPIHIALNFSLDPQA
CCEEEEEECCCCCCC		18.5522451694
658N-linked_GlycosylationCVPDLQLEVFGEQNH
ECCCEEEEEECCCCE		23.8822451694
672N-linked_GlycosylationHVYLGDKNALNLTFH
EEEECCCCEEEEEEE		55.17-
675N-linked_GlycosylationLGDKNALNLTFHAQN
ECCCCEEEEEEEEEE		34.3219159218
682N-linked_GlycosylationNLTFHAQNVGEGGAY
EEEEEEEECCCCCEE		44.5419349973
712N-linked_GlycosylationGLVRHPGNFSSLSCD
CCCCCCCCCCCCCCC		37.7717660510
721N-linked_GlycosylationSSLSCDYFAVNQSRL
CCCCCCEEEECCCEE		3.8019349973
724N-linked_GlycosylationSCDYFAVNQSRLLVC
CCCEEEECCCEEEEE		30.5817660510
724N-linked_GlycosylationSCDYFAVNQSRLLVC
CCCEEEECCCEEEEE		30.5819349973
731N-linked_GlycosylationNQSRLLVCDLGNPMK
CCCEEEEEECCCCCC		3.4519349973
731S-nitrosylationNQSRLLVCDLGNPMK
CCCEEEEEECCCCCC		3.4525040305
742PhosphorylationNPMKAGASLWGGLRF
CCCCCCCHHCCCEEE		24.6021406692
760PhosphorylationHLRDTKKTIQFDFQI
CCCCCCCEEEEEHHH		22.9021406692
769PhosphorylationQFDFQILSKNLNNSQ
EEEHHHHHHCCCCCC		22.5624719451
771N-linked_GlycosylationDFQILSKNLNNSQSD
EHHHHHHCCCCCCCC		44.6219349973
773N-linked_GlycosylationQILSKNLNNSQSDVV
HHHHHCCCCCCCCEE		56.3417660510
774N-linked_GlycosylationILSKNLNNSQSDVVS
HHHHCCCCCCCCEEE		44.5919349973
791PhosphorylationLSVEAQAQVTLNGVS
EEEEEEEEEEECCCC		19.35-
820N-linked_GlycosylationRDQPQKEEDLGPAVH
CCCCCCHHHCHHHHH		66.6219349973
822N-linked_GlycosylationQPQKEEDLGPAVHHV
CCCCHHHCHHHHHHH		11.3619349973
822N-linked_GlycosylationQPQKEEDLGPAVHHV
CCCCHHHCHHHHHHH		11.3619349973
823N-linked_GlycosylationPQKEEDLGPAVHHVY
CCCHHHCHHHHHHHH		22.0519349973
868N-linked_GlycosylationVTRVTGLNCTTNHPI
EEEECCCCCCCCCCC		23.57UniProtKB CARBOHYD
887PhosphorylationLELDPEGSLHHQQKR
CEECCCCCCCCCCCC		23.91-
901O-linked_GlycosylationREAPSRSSASSGPQI
CCCCCCCCCCCCCCE		30.93OGP
943UbiquitinationLHFRVWAKTFLQREH
HHHHHHHHHHHHHCC		24.89-
992UbiquitinationAVQWTKAEGSYGVPL
HHHHHHCCCCCHHHH		50.67-
1038UbiquitinationPYGTAMEKAQLKPPA
CCCCHHHHCCCCCCC		28.48-
1042UbiquitinationAMEKAQLKPPATSDA
HHHHCCCCCCCCCCC		36.5521906983
1046PhosphorylationAQLKPPATSDA----
CCCCCCCCCCC----		32.6723403867
1047PhosphorylationQLKPPATSDA-----
CCCCCCCCCC-----		33.3823403867
1091Ubiquitination-------------------------------------------------
-------------------------------------------------		-
1096Phosphorylation------------------------------------------------------
------------------------------------------------------		-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:15728256
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA5_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ITA5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ILK_HUMANILKphysical
8538749
CD9_HUMANCD9physical
10065872
GIPC1_HUMANGIPC1physical
11479315
MSS4_HUMANRABIFphysical
10094488
FGFR2_HUMANFGFR2physical
15728256
UBC_HUMANUBCphysical
15728256
FINC_HUMANFN1physical
20643357
ITB1_HUMANITGB1physical
20643357
SHRPN_HUMANSHARPINphysical
21947080
ITB1_HUMANITGB1physical
21947080
ITB1_HUMANITGB1physical
22939629
STABP_HUMANSTAMBPphysical
21988832
SE1L1_HUMANSEL1Lphysical
24324549
ITB1_HUMANITGB1physical
26344197
ITB3_HUMANITGB3physical
26344197
LG3BP_HUMANLGALS3BPphysical
24362527
ITB3_HUMANITGB3physical
10358085
CIB1_HUMANCIB1physical
24163826
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D06319 Volociximab (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITA5_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-307; ASN-771 ANDASN-773, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297; ASN-307; ASN-675 ANDASN-773, AND MASS SPECTROMETRY.

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